Biology, 24.04.2020 19:44 122333444469
Serine 14 of glycogen phosphorylase was replaced by glutamate in an experiment. The Vmax of the mutant enzyme was compared to wild type phosphorylase a and b.
Wild type phosphorylase a 100 ± 5
Wild type phosphorylase b 25 ± 0.4
Serine (S) to Glutamate (E) mutant 60 ± 3
Explain the results obtained with the S to E mutant glycogen phosphorylase.
a) Glutamate positively charged R group mimics the phosphoryl group on serine. There is a reduced response because the carboxyl group is smaller and less charged than the phosphate.
b) Glutamate negatively charged R group mimics a phosphorylated serine residue. The VmaxVmax is reduced because the carboxyl group is smaller and less charged than a phosphate group.
c) The S to E mutant would mimic the phosphorylase in the T state. The reduced response is due to blockage of phosphorylase kinase’s catalytic site.
d) The S to E mutant would mimic the phosphorylase in the R state. The reduced response is due to blockage of phosphorylase kinase’s catalytic site.
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